Biophysical characterization of G protein ectodomain of group B human respiratory syncytial virus from E. coli |
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Authors: | Wajihul Hasan Khan V L N Raghuram Srungaram Asimul Islam Ilyas Beg Md Shakir H Haider Faizan Ahmad |
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Institution: | 1. Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India;2. Department of Microbiology, All India Institute of Medical Sciences, New Delhi, India |
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Abstract: | Human respiratory syncytial virus (hRSV) is an important pathogen of acute respiratory tract infection. The G protein of hRSV is a transmembrane glycoprotein that is a neutralizing antigen and is thus a vaccine candidate. In this study, synthetic codon optimized ectodomain G protein G(ΔTM)] of BA genotype of group B hRSV was cloned, expressed, and characterized using biophysical techniques. The molar absorption coefficient and mean residue ellipticity at 222 nm (θ]222) of G (ΔTM) was found to be 7950 M?1 cm?1 and ?19701.7 deg cm2 dmol-1 respectively. It was concluded that G(ΔTM) mainly consist of α-helix (74.9%) with some amount of β-sheet (4%). The protein was stable up to 85°C without any transition curve. However, heat-induced denaturation of G(ΔTM) resulted in total loss of β-sheet whereas not much change was observed in the α-helix part of the secondary structure. It was concluded that G(ΔTM) is an α-helical protein and it is highly stable at high temperature, but could be easily denatured using high concentrations of GdmCl/urea or acidic condition. This is the first investigation of cloning, expression, and characterization of G(ΔTM) of BA viruses from India. Structural characterization of G protein will assist in drug designing and vaccine development for hRSV. |
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Keywords: | BA genotype biophysical characterization ectodomain G protein human respiratory syncytial virus |
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